The Journal of Experimental Medicine
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Published online 18 December 2000.
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© The Rockefeller University Press, 0022-1007/2000/12/1697/ $5.00
The Journal of Experimental Medicine, Volume 192, Number 12, December 18, 2000 1697-1706

Original Article

Hla-Dm Recognizes the Flexible Conformation of Major Histocompatibility Complex Class II

Chih-Ling Choub and Scheherazade Sadegh-Nasseria,b

a Department of Pathology, Johns Hopkins University School of Medicine, Baltimore, Maryland 21205
b Graduate Program in Molecular Biophysics, Johns Hopkins University School of Medicine, Baltimore, Maryland 21205
Department of Pathology, Johns Hopkins University School of Medicine, 664E Ross Building, Baltimore, MD 21205.410-614-3548410-614-4931

ssadegh{at}jhmi.edu

DM facilitates formation of high affinity complexes of peptide–major histocompatibility complex (MHC) by release of class II MHC–associated invariant chain peptide (CLIP). This has been proposed to occur through discrimination of complex stability. By probing kinetic and conformational intermediates of the wild-type and mutant human histocompatibility leukocyte antigen (HLA)-DR1–peptide complexes, and examining their reactivities with DM, we propose that DM interacts with the flexible hydrophobic pocket 1 of DR1 and converts the molecule into a conformation that is highly peptide receptive. A more rigid conformation, generated upon filling of pocket 1, is less susceptible to DM effects. Thus, DM edits peptide–MHC by recognition of the flexibility rather than stability of the complex.

Key Words: antigen processing • molecular conformation • HLA-DR antigens • surface plasmon resonance • fluorometry

Abbreviations used in this paper: AMCA, 7-amino-4-methyl-coumarin-3-acetic acid; CLIP, class II MHC–associated invariant chain peptide; HA, hemagglutinin; RU, resonance unit; SPR, surface plasmon resonance; wt, wild-type.

© 2000 The Rockefeller University Press


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